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P35128

- UBE2N_DROME

UniProt

P35128 - UBE2N_DROME

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Protein

Ubiquitin-conjugating enzyme E2 N

Gene

ben

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Catalyzes the covalent attachment of ubiquitin to other proteins.

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei87 – 871Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. ubiquitin conjugating enzyme binding Source: FlyBase
  4. ubiquitin protein ligase binding Source: FlyBase
  5. ubiquitin-protein transferase activity Source: FlyBase

GO - Biological processi

  1. axonogenesis Source: FlyBase
  2. axon target recognition Source: FlyBase
  3. flight behavior Source: FlyBase
  4. grooming behavior Source: FlyBase
  5. jump response Source: FlyBase
  6. photoreceptor cell morphogenesis Source: FlyBase
  7. positive regulation of mitotic cell cycle, embryonic Source: FlyBase
  8. protein polyubiquitination Source: FlyBase
  9. response to anesthetic Source: FlyBase
  10. synapse maturation Source: FlyBase
  11. synaptic growth at neuromuscular junction Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_180724. ISG15 antiviral mechanism.
REACT_181705. Interleukin-1 signaling.
REACT_268843. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_270342. IRAK1 recruits IKK complex.
SignaLinkiP35128.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 N (EC:6.3.2.19)
Alternative name(s):
Protein bendless
Ubiquitin carrier protein N
Ubiquitin-conjugating enzyme E2-17 kDa
Ubiquitin-protein ligase D3
Ubiquitin-protein ligase N
Gene namesi
Name:ben
Synonyms:UbcD3
ORF Names:CG18319
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0000173. ben.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: FlyBase
  2. perinuclear region of cytoplasm Source: FlyBase
  3. UBC13-UEV1A complex Source: FlyBase
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Mutants in this gene exhibit several, largely neuronal defects including lesions affecting the neuronal connectivity of the giant fiber with the "jumping muscle", and the axons of photoreceptor cells R7 and R8 fail to make the proper right-angle turn into the medulla (hence the term "bendless").1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 151151Ubiquitin-conjugating enzyme E2 NPRO_0000082521Add
BLAST

Proteomic databases

PaxDbiP35128.
PRIDEiP35128.

Expressioni

Gene expression databases

BgeeiP35128.
ExpressionAtlasiP35128. differential.

Interactioni

Protein-protein interaction databases

BioGridi58728. 4 interactions.
DIPiDIP-22866N.
MINTiMINT-1003000.
STRINGi7227.FBpp0289793.

Structurei

3D structure databases

ProteinModelPortaliP35128.
SMRiP35128. Positions 4-149.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00540000070023.
InParanoidiP35128.
KOiK10580.
OMAiDVAKHYK.
OrthoDBiEOG7XWPQB.
PhylomeDBiP35128.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35128-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSLPRRIIK ETQRLMQEPV PGINAIPDEN NARYFHVIVT GPNDSPFEGG
60 70 80 90 100
VFKLELFLPE DYPMSAPKVR FITKIYHPNI DRLGRICLDV LKDKWSPALQ
110 120 130 140 150
IRTILLSIQA LLSAPNPDDP LANDVAELWK VNEAEAIRNA REWTQKYAVE

D
Length:151
Mass (Da):17,236
Last modified:February 1, 1994 - v1
Checksum:i1D096E72A7AEA420
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20126 mRNA. Translation: AAA28392.1.
S70118 mRNA. Translation: AAB30753.1.
EU217226 Genomic DNA. Translation: ABW92183.1.
EU217227 Genomic DNA. Translation: ABW92184.1.
EU217228 Genomic DNA. Translation: ABW92185.1.
EU217229 Genomic DNA. Translation: ABW92186.1.
EU217230 Genomic DNA. Translation: ABW92187.1.
EU217231 Genomic DNA. Translation: ABW92188.1.
EU217232 Genomic DNA. Translation: ABW92189.1.
EU217233 Genomic DNA. Translation: ABW92190.1.
EU217234 Genomic DNA. Translation: ABW92191.1.
EU217235 Genomic DNA. Translation: ABW92192.1.
EU217236 Genomic DNA. Translation: ABW92193.1.
EU217237 Genomic DNA. Translation: ABW92194.1.
AE014298 Genomic DNA. Translation: AAF48338.1.
AY069527 mRNA. Translation: AAL39672.1.
PIRiS35793.
RefSeqiNP_001162752.1. NM_001169281.2.
NP_001245663.1. NM_001258734.2.
NP_001259540.1. NM_001272611.2.
NP_001259541.1. NM_001272612.2.
NP_511150.1. NM_078595.3.
UniGeneiDm.2088.

Genome annotation databases

EnsemblMetazoaiFBtr0073855; FBpp0073686; FBgn0000173.
FBtr0300566; FBpp0289793; FBgn0000173.
FBtr0307296; FBpp0298297; FBgn0000173.
FBtr0332843; FBpp0305066; FBgn0000173.
FBtr0332844; FBpp0305067; FBgn0000173.
GeneIDi32358.
KEGGidme:Dmel_CG18319.
UCSCiCG18319-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20126 mRNA. Translation: AAA28392.1 .
S70118 mRNA. Translation: AAB30753.1 .
EU217226 Genomic DNA. Translation: ABW92183.1 .
EU217227 Genomic DNA. Translation: ABW92184.1 .
EU217228 Genomic DNA. Translation: ABW92185.1 .
EU217229 Genomic DNA. Translation: ABW92186.1 .
EU217230 Genomic DNA. Translation: ABW92187.1 .
EU217231 Genomic DNA. Translation: ABW92188.1 .
EU217232 Genomic DNA. Translation: ABW92189.1 .
EU217233 Genomic DNA. Translation: ABW92190.1 .
EU217234 Genomic DNA. Translation: ABW92191.1 .
EU217235 Genomic DNA. Translation: ABW92192.1 .
EU217236 Genomic DNA. Translation: ABW92193.1 .
EU217237 Genomic DNA. Translation: ABW92194.1 .
AE014298 Genomic DNA. Translation: AAF48338.1 .
AY069527 mRNA. Translation: AAL39672.1 .
PIRi S35793.
RefSeqi NP_001162752.1. NM_001169281.2.
NP_001245663.1. NM_001258734.2.
NP_001259540.1. NM_001272611.2.
NP_001259541.1. NM_001272612.2.
NP_511150.1. NM_078595.3.
UniGenei Dm.2088.

3D structure databases

ProteinModelPortali P35128.
SMRi P35128. Positions 4-149.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 58728. 4 interactions.
DIPi DIP-22866N.
MINTi MINT-1003000.
STRINGi 7227.FBpp0289793.

Proteomic databases

PaxDbi P35128.
PRIDEi P35128.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0073855 ; FBpp0073686 ; FBgn0000173 .
FBtr0300566 ; FBpp0289793 ; FBgn0000173 .
FBtr0307296 ; FBpp0298297 ; FBgn0000173 .
FBtr0332843 ; FBpp0305066 ; FBgn0000173 .
FBtr0332844 ; FBpp0305067 ; FBgn0000173 .
GeneIDi 32358.
KEGGi dme:Dmel_CG18319.
UCSCi CG18319-RA. d. melanogaster.

Organism-specific databases

CTDi 32358.
FlyBasei FBgn0000173. ben.

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00540000070023.
InParanoidi P35128.
KOi K10580.
OMAi DVAKHYK.
OrthoDBi EOG7XWPQB.
PhylomeDBi P35128.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_180724. ISG15 antiviral mechanism.
REACT_181705. Interleukin-1 signaling.
REACT_268843. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_270342. IRAK1 recruits IKK complex.
SignaLinki P35128.

Miscellaneous databases

GenomeRNAii 32358.
NextBioi 778098.

Gene expression databases

Bgeei P35128.
ExpressionAtlasi P35128. differential.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila bendless gene encodes a neural protein related to ubiquitin-conjugating enzymes."
    Muralidhar M., Thomas J.B.
    Neuron 11:253-266(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE.
  2. "Bendless, a Drosophila gene affecting neuronal connectivity, encodes a ubiquitin-conjugating enzyme homolog."
    Oh C.E., McMahon R., Benzer S., Tanouye M.A.
    J. Neurosci. 14:3166-3179(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Hitchhiking effects of recurrent beneficial amino acid substitutions in the Drosophila melanogaster genome."
    Andolfatto P.
    Genome Res. 17:1755-1762(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ZW104, ZW109, ZW122, ZW123, ZW133, ZW136, ZW139, ZW140, ZW141, ZW142, ZW143 and ZW144.
  4. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiUBE2N_DROME
AccessioniPrimary (citable) accession number: P35128
Secondary accession number(s): A9YHJ7, Q9VY67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 26, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3